3ear: Difference between revisions

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==Novel dimerization motif in the DEAD box RNA helicase Hera: form 1, partial dimer==
==Novel dimerization motif in the DEAD box RNA helicase Hera: form 1, partial dimer==
<StructureSection load='3ear' size='340' side='right' caption='[[3ear]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3ear' size='340' side='right'caption='[[3ear]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ear]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ear]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eaq|3eaq]], [[3eas|3eas]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eaq|3eaq]], [[3eas|3eas]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1895 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1895 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ear FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ear OCA], [http://pdbe.org/3ear PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ear RCSB], [http://www.ebi.ac.uk/pdbsum/3ear PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ear ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ear FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ear OCA], [https://pdbe.org/3ear PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ear RCSB], [https://www.ebi.ac.uk/pdbsum/3ear PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ear ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3ear_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3ear_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</div>
</div>
<div class="pdbe-citations 3ear" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3ear" style="background-color:#fffaf0;"></div>
==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Thet2]]
[[Category: Thet2]]
[[Category: Klostermeier, D]]
[[Category: Klostermeier, D]]

Revision as of 14:45, 16 February 2022

Novel dimerization motif in the DEAD box RNA helicase Hera: form 1, partial dimerNovel dimerization motif in the DEAD box RNA helicase Hera: form 1, partial dimer

Structural highlights

3ear is a 2 chain structure with sequence from Thet2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:TT_C1895 (THET2)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.

A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.,Klostermeier D, Rudolph MG Nucleic Acids Res. 2009 Feb;37(2):421-30. Epub 2008 Dec 2. PMID:19050012[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Klostermeier D, Rudolph MG. A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility. Nucleic Acids Res. 2009 Feb;37(2):421-30. Epub 2008 Dec 2. PMID:19050012 doi:10.1093/nar/gkn947

3ear, resolution 2.30Å

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OCA